1cj5
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(New page: 200px<br /><applet load="1cj5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cj5" /> '''BOVINE BETA-LACTOGLOBULIN A'''<br /> ==Over...)
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Revision as of 10:23, 20 November 2007
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BOVINE BETA-LACTOGLOBULIN A
Overview
Using heteronuclear NMR spectroscopy, we studied the solution structure, and dynamics of bovine beta-lactoglobulin A at pH 2.0 and 45 degrees C, where the protein exists as a monomeric native state. The monomeric NMR, structure, comprising an eight-stranded continuous antiparallel, beta-barrel and one major alpha-helix, is similar to the X-ray dimeric, structure obtained at pH 6.2, including betaI-strand that forms the dimer, interface and loop EF that serves as a lid of the interior hydrophobic, hole. [1H]-15N NOE revealed that betaF, betaG, and betaH strands buried, under the major alpha-helix are rigid on a pico- to nanosecond time scale, and also emphasized rapid fluctuations of loops and the N- and C-terminal, regions.
About this Structure
1CJ5 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Solution structure and dynamics of bovine beta-lactoglobulin A., Kuwata K, Hoshino M, Forge V, Era S, Batt CA, Goto Y, Protein Sci. 1999 Nov;8(11):2541-5. PMID:10595563
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